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Mutant of human tissue type plasminogen activator

A plasminogen and mutant technology, applied in the field of peptides, can solve the problems of high cost, unimproved thrombolytic specificity, large dose and the like

Inactive Publication Date: 2004-05-19
李宝健 +2
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Problems solved by technology

But there are following defects: the half-life in the blood in the human body is very short, which is mainly due to the rapid and specific In addition, h-tPA can also bind to specific receptors on human liver parenchyma and hepatic cortical cells to be phagocytized and cleared from the blood
Therefore, when h-tPA is used as a drug, the dose required is particularly high, resulting in high cost
On the other hand, the thrombolytic specificity of h-tPA needs to be improved
[0003] Judging from the current relevant literature and h-tPA mutants that have been marketed, although their half-life is longer than that of h-tPA, a simpler and lower-dose treatment plan can be used, but their thrombolytic specificity has not been obtained. improved, so its efficacy did not exceed that of h-tPA
Moreover, the mutation sites of h-tPA mutants reported so far are very limited

Method used

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  • Mutant of human tissue type plasminogen activator
  • Mutant of human tissue type plasminogen activator
  • Mutant of human tissue type plasminogen activator

Examples

Experimental program
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Embodiment Construction

[0082] The schematic diagram of the primary structure of the human tissue plasminogen activator mutant in this example is as follows figure 1 As shown, its construction method is as follows:

[0083] Using RT-PCR technology, a 1.73 KB fragment was amplified from human melanoma total RNA with primer 5'-AGGGACGCTGTGAAGCAATC-3' and primer 5'-TTTGAGGAGTCGGGTGTTCC-3'. It was connected with the pGEM-T vector, transformed into Escherichia coli JM109, and the recombinant plasmid pGEM-tPA was obtained. In order to obtain single-stranded DNA for mutagenesis, the h-tPA cDNA needs to be cloned into phagemid pTZl9U. The pGEM-tPA plasmid was first digested with Nco I, then the cohesive ends were filled in with Escherichia coli DNA polymerase Klenow fragment, and finally digested with Sal I. The 1.7 kb fragment was recovered, connected to the linear pTZ19U vector digested with BamH I, blunted with Escherichia coli DNA polymerase Klenow fragment, and then digested with Sal I, and transforme...

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Abstract

A human tissue type plasminogen activator mutant features that in the h-tPA is its amino acid sequence, the Leu at site 66, the Tyr at site 67, the asparamides at sites 117 and 184 and the lys at site 416 are respectively replaced by Ala, Ser, glutamine and Tyr, and 7 amino acids at sites 296-302 are removed. Its advantages are longer half-lift period and higher thrombolytic specificity.

Description

Technical field [0001] The present invention relates to a polypeptide with potential curative effect on human thrombotic diseases, in particular to human tissue type plasminogen activator mutant. Background technique [0002] Human tissue plasminogen activator (human tissue plasminogen activator, referred to as h-tPA, refers to the mature natural human tissue plasminogen activator protein molecule, the same below) is currently internationally recognized as the best curative treatment Biomacromolecular Drugs for Thrombotic Diseases. But there are following defects: the half-life in the blood in the human body is very short, which is mainly due to the rapid and specific In addition, h-tPA can also bind to specific receptors on human liver parenchyma and hepatic cortical cells to be phagocytosed and cleared from the blood. Therefore, when h-tPA is used as a medicine, the dosage required is particularly large, resulting in high cost. On the other hand, the thrombolytic specif...

Claims

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Application Information

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IPC IPC(8): A61P7/02C07K14/435C07K14/47C12N9/72C12N15/58
Inventor 李宝健刘军波陆阳
Owner 李宝健
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